eF-site ID 1bcc-ABCDEFGHIJ PDB Code 1bcc Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title CYTOCHROME BC1 COMPLEX FROM CHICKEN Classification OXIDOREDUCTASE Compound UBIQUINOL CYTOCHROME C OXIDOREDUCTASE Source ORGANISM_COMMON: chicken; ORGANISM_SCIENTIFIC: Gallus gallus; Sequence A:  YAQALQSVPETQVSQLDNGVRVASEQSSQPTCTVGVWIDA GSRYESEKNNGAGYFLEHLAFKGTKNRPQNALEKEVESMG AHLNAYSSREHTAYYIKALSKDVPKAVELLADIVQNCSLE DSQIEKERDVIVRELQENDTSMREVVFNYLHATAFQGTGL AQSVEGPSENIRKLSRADLTEYLSTHYTAPRMVLAAAGGV EHQQLLELAQKHFGGVPFTYDDDAVPTLSKCRFTGSQIRH REDGLPLAHVAIAVEGPGWAHPDLVALQVANAIIGHYDRT YGGGLHSSSPLASIAVTNKLCQSFQTFSICYSETGLFGFY FVCDRMSIDDMMFVLQGQWMRLCTSISESEVLRGKNFLRN ALVSHLDGTTPVCEDIGRELLTYGRRIPLEEWEERLAEVD ARMVREVCSKYIYDQCPAVAGPGPIEQLPDYNRIRSGMFW LR B:  PPHPQDLEITKLPNGLVIASLENYSPGSTIGVFIKAGSRY ENSSNLGTSHLLRLASSLTTKGASSFKITRGIEAVGGKLS VESTRENMAYTVECLRDDVEILMEFLLNVTTAPEFRPWEV ADLQPQLKIDKAVAFQNPQTHVIENLHAAAYRNALADSLY CPDYRIGKVTSVELHDFVQNHFTSARMALVGLGVSHPVLK NVAEQLLNIRGGLGLSGAKAKYRGGEIREQNGDSLVHAAI VAESAAIGGAEANAFSVLQHVLGANPHVKRGNPFDVSAFN ASYSDSGLFGFYTISQAAYAGQVIKAAYNQVKTIAQGNVS NENVQAAKNKLKAKYLMSVESSEGFLEEVGSQALAAGSYN PPSTVLQQIDAVADADVIKAAKKFVSRQKSMAASGNLGHT PFVDEL C:  APNIRKSHPLLKMINNSLIDLPAPSNISAWWNFGSLLAVC LMTQILTGLLLAMHYTADTSLAFSSVAHTCRNVQYGWLIR NLHANGASFFFICIFLHIGRGLYYGSYLYKETWNTGVILL LTLMATAFVGYVLPWGQMSFWGATVITNLFSAIPYIGHTL VEWAWGGFSVDNPTLTRFFALHFLLPFAIAGITIIHLTFL HESGSNNPLGISSDSDKIPFHPYYSFKDILGLTLMLTPFL TLALFSPNLLGDPENFTPANPLVTPPHIKPEWYFLFAYAI LRSIPNKLGGVLALAASVLILFLIPFLHKSKQRTMTFRPL SQTLFWLLVANLLILTWIGSQPVEHPFIIIGQMASLSYFT ILLILFPTIGTLENKMLNY D:  SDLELHPPSYPWSHRGPLSSLDHTSIRRGFQVYKQVCSSC HSMDYVAYRHLVGVCYTEDEAKALAEEVEVQDGPNEDGEM FMRPGKLSDYFPKPYPNPEAARAANNGALPPDLSYIVRAR HGGEDYVFSLLTGYCEPPTGVSVREGLYFNPYFPGQAIGM APPIYNDVLEFDDGTPATMSQVAKDVCTFLRWAAEPEHDH RKRMGLKMLLMMGLLVPLVYYMKRHKWSVLKSRKLAYRPP K E:  SHTDIKVPNFSDYRRPPDDYSTKSSRESDPSRKGFSYLVT AVTTLGVAYAAKNVVTQFVSSMSASADVLAMSKIEIKLSD IPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDP QHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPC HGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG F:  SRWLEGIRKWYYNAAGFNKYGLMRDDTIYENDDVKEAIRR LPENLYDDRMFRIKRALDLNMRQQILPKEQWTKYEEDVPY LEPYLKEVIRERKEREEWDK G:  RQFGHLTRVRHLITYSLSPFEQRPFPHYFSKGVPNVWRRL RACILRVAPPFLAFYLLYTWGTQEFEKSKRKNPAAYVN H:  LVDPLTTVREQCEQLEKCVKARERLELCDERVSSRSQTEE DCTEELFDFLHARDHCVAHKLFNSLK I:  XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX J:  TLTARLYSLLFRRTSTFALTIVVGALLFERAFDQGADAIY EHINEGKLWKHIKHKYENK Description (1)  UBIQUINOL CYTOCHROME C OXIDOREDUCTASE, PROTOPORPHYRIN IX CONTAINING FE, FE2/S2 (INORGANIC) CLUSTER, UBIQUINONE-10, HEPTADEC-12-ENOIC ACID 3-[(2-AMINO-ETHYL)-PHOSPHOHYDROXY]- 2-HEXADEC-11-ENYLOXYMETHOXY-9-PROPYL ESTER Functional site 1) chain C residue 84 type sequence H description HISTIDINE AXIAL LIGANDS OF LOW POTENTIAL HEME OF CYTOCHROME B. source : BLO 2) chain C residue 183 type sequence H description HISTIDINE AXIAL LIGANDS OF LOW POTENTIAL HEME OF CYTOCHROME B. source : BLO 3) chain C residue 98 type sequence H description HISTIDINE AXIAL LIGANDS OF HIGH POTENTIAL HEME OF CYTOCHROME B. source : BHI 4) chain C residue 197 type sequence H description HISTIDINE AXIAL LIGANDS OF HIGH POTENTIAL HEME OF CYTOCHROME B. source : BHI 5) chain D residue 41 type sequence H description HISTIDINE AND METHIONINE AXIAL LIGANDS OF HIGH POTENTIAL HEME OF CYTOCHROME C1. source : C1H 6) chain D residue 160 type sequence M description HISTIDINE AND METHIONINE AXIAL LIGANDS OF HIGH POTENTIAL HEME OF CYTOCHROME C1. source : C1H 7) chain E residue 139 type sequence C description HISTIDINE AND CYSTINE LIGANDS OF THE RIESKE IRON-SULFUR CLUSTER. source : FES 8) chain E residue 141 type sequence H description HISTIDINE AND CYSTINE LIGANDS OF THE RIESKE IRON-SULFUR CLUSTER. source : FES 9) chain E residue 158 type sequence C description HISTIDINE AND CYSTINE LIGANDS OF THE RIESKE IRON-SULFUR CLUSTER. source : FES 10) chain E residue 161 type sequence H description HISTIDINE AND CYSTINE LIGANDS OF THE RIESKE IRON-SULFUR CLUSTER. source : FES 11) chain D residue 124 type TOPO_DOM sequence E description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 12) chain C residue 114-134 type TOPO_DOM sequence WNTGVILLLTLMATAFVGYVL description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 13) chain C residue 179-199 type TOPO_DOM sequence FFALHFLLPFAIAGITIIHLT description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 14) chain C residue 227-247 type TOPO_DOM sequence FKDILGLTLMLTPFLTLALFS description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 15) chain C residue 289-309 type TOPO_DOM sequence LGGVLALAASVLILFLIPFLH description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 16) chain C residue 321-341 type TOPO_DOM sequence LSQTLFWLLVANLLILTWIGS description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 17) chain C residue 348-368 type TOPO_DOM sequence FIIIGQMASLSYFTILLILFP description Mitochondrial matrix => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI1 18) chain J residue 22-47 type TRANSMEM sequence LTIVVGALLFERAFDQGADAIYEHIN description Helical => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI2 19) chain F residue 83 type TRANSMEM sequence Y description Helical => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI2 20) chain F residue 96 type TRANSMEM sequence E description Helical => ECO:0000269|PubMed:9651245 source Swiss-Prot : SWS_FT_FI2 21) chain G residue 33 type MOD_RES sequence G description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ69 source Swiss-Prot : SWS_FT_FI3 22) chain F residue 88 type MOD_RES sequence P description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CQ69 source Swiss-Prot : SWS_FT_FI3 23) chain E residue 139 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 24) chain E residue 141 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 25) chain E residue 158 type BINDING sequence C description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 26) chain E residue 161 type BINDING sequence H description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 27) chain E residue 163 type BINDING sequence S description BINDING => ECO:0000269|PubMed:9651245, ECO:0007744|PDB:1BE3, ECO:0007744|PDB:1BGY source Swiss-Prot : SWS_FT_FI4 28) chain B residue 54-77 type prosite sequence GSRYENSSNLGTSHLLRLASSLTT description INSULINASE Insulinase family, zinc-binding region signature. GsryenssnlGtSHLLRLAsSlTT source prosite : PS00143 29) chain C residue 202 type BINDING sequence H description BINDING => ECO:0000269|PubMed:21575592, ECO:0000269|PubMed:22690928, ECO:0000269|PubMed:9565029, ECO:0007744|PDB:1BCC, ECO:0007744|PDB:3CWB, ECO:0007744|PDB:3H1K, ECO:0007744|PDB:3L72 source Swiss-Prot : SWS_FT_FI5

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